(1) Experiments designed to test the direct transfer mechanism for metabolites in the glycolytic pathway have revealed that the data used to support the proposed mechanism are questionable. Contrary to the report that aldolase forms a complex with alpha- glycerol-3-phosphate dehydrogenase and facilitates the dehydrogenase catalyzed reaction through direct transfer of aldolase-bound substrate, dihydroxyacetone phosphate, we found that aldolase inhibits the dehydrogenase-catalyzed reaction by removing substrate for alpha-glycerol-3-phosphate dehydrogenase. In addition, transient kinetic data show that the reported first-ordered transfer rate of NADH from alpha- glycerol-3-phosphate dehydrogenase to lactate dehydrogenase is a composite of two reactions, one due to free NADH binding to lactate dehydrogenase and the other due to complex formation between the two dehydrogenases. (2) Binding constants for Ca(II) and a number of divalent metal ions have been determined for a family of Ca(II) indicators designed to probe intracellular calcium concentration. (3) A theory has been developed to account for the effect of oscillating of fluctuating membrane potential on the function of membrane-bound proteins. The theory provides a reasonable mechanism for energy transduction. In addition, an oscillating electric pulse apparatus is being constructed to carry out experiments to test the validity of the theory. (4) Work is in progress to purify and characterize isopeptidase.